ArticleThe journal of physical chemistry letters2013
Hysteresis as a Marker for Complex, Overlapping Landscapes in Proteins.
Article in The journal of physical chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- Article
- Folding pathway of a discontinuous two-domain protein.Nature communications · 2024Article
- A Marcus-Type Inverted Region in the Translocation Kinetics of a Knotted Protein.The journal of physical chemistry letters · 2023Article
- AlphaFold predicts novel human proteins with knots.Protein science : a publication of the Protein Society · 2023Article
- Hysteresis behavior in the unfolding/refolding processes of a protein trapped in metallo-cages.Chemical science · 2023Article
- Growth Rate and Thermal Properties of DNA Origami Filaments.Nano letters · 2022Article
- Modeling ATP-mediated endothelial cell elongation on line patterns.Biomechanics and modeling in mechanobiology · 2022Article
- Revealing Topological Barriers against Knot Untying in Thermal and Mechanical Protein Unfolding by Molecular Dynamics Simulations.Biomolecules · 2021Article
- Characterization of the structural forces governing the reversibility of the thermal unfolding of the human acidic fibroblast growth factor.Scientific reports · 2021Article
- Theory and applications of differential scanning fluorimetry in early-stage drug discovery.Biophysical reviews · 2020Review
- Single-Molecule Mechanistic Study of Enzyme Hysteresis.ACS central science · 2019Article
- Thermal unfolding and refolding of a lytic polysaccharide monooxygenase fromRSC advances · 2019Article
- Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.Biophysical journal · 2019Article
- The AAA+ protease ClpXP can easily degrade a 3Scientific reports · 2019Article
- To Tie or Not to Tie? That Is the Question.Polymers · 2017Review
- Topological transformations in proteins: effects of heating and proximity of an interface.Scientific reports · 2017Article
- Negative Charge Neutralization in the Loops and Turns of Outer Membrane Phospholipase A Impacts Folding Hysteresis at Neutral pH.Biochemistry · 2016Article
- Untangling the Influence of a Protein Knot on Folding.Biophysical journal · 2016Article
- N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry.The Journal of biological chemistry · 2015Article
- Heterogeneous side chain conformation highlights a network of interactions implicated in hysteresis of the knotted protein, minimal tied trefoil.Journal of physics. Condensed matter : an Institute of Physics journal · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Topologically complex proteins fold by multiple routes as a result of hard-to-fold regions of the proteins. Oftentimes these regions are introduced into the protein scaffold for function and increase frustration in the otherwise smooth-funneled landscape. Interestingly, while functional regions add complexity to folding landscapes, they may also contribute to a unique behavior referred to as hysteresis. While hysteresis is predicted to be rare, it is observed in various proteins, including proteins containing a unique peptide cyclization to form a fluorescent chromophore as well as proteins containing a knotted topology in their native fold. Here, hysteresis is demonstrated to be a consequence of the decoupling of unfolding events from the isomerization or hula-twist of a chromophore in one protein and the untying of the knot in a second protein system. The question now is- can hysteresis be a marker for the interplay of landscapes where complex folding and functional regions overlap?
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.